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Introduction of the effect of the concentration of enzyme peroxidase, ph, temperature, inhibitor at their different levels on the peroxidase reaction
Experiment of study of enzyme peroxidase
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Research on the Optimal Environment for Peroxidase to Survive with a focus on Temperature, pH, and Concentration Introduction Enzymes play a major role in virtually every single ecosystem as a conductor of reactions. They are important because without them reactions that need to take place in these cells would occur to slowly for DNA replication to occur as well as other reactions. The enzyme chosen for this experiments was peroxidase. “Peroxiredoxins (Prx), regulate the intracellular concentration of H2O2 by reducing it in the presence of an appropriate electron donor.” (Choi et al.). Enzymes are organic molecules that are made up of a string of carbons oxygens and hydrogens. The main component of bonding in these strings of molecules is …show more content…
The experiment will test the reactivity of various proteins, and such is determined by the change in color of the solution. The change in color of this solution occurred due to the addition of the guaiacol dye that reacted alongside the peroxidase. First, the amount of peroxidase solution used in each test needed to be constant, so we had to determine the optimum amount of solution to use. It was important to use accurate and precise data, so pipets were used to make sure the data was consistent. Through aligning seven test tubes, each with varying amounts of the peroxidase (.5mL, 1mL, 2mL) we found at which point the peroxidase is the most productive. By adding each solution to a spectrophotometer, we were able to determine the point at which the enzyme was the most absorbent, which in this case was 2mL, and this was carried though the whole …show more content…
Eleven clean test tubes were obtained, and reagents with the exact amount of buffer, hydrogen peroxide, peroxidase, and guaiacol were all mixed and spread out over the eleven test tubes in 5 segments. The Buffer and the peroxidase were in one tube while the hydrogen peroxide and the Guaiacol were in another. These were then exposed to water baths of varying interval temperatures at 4, 22, 45, 60, 100 Celsius. Once the solutions had reached their specified temperature, they were mixed together and immediately were tested with the spectrophotometer. The results were recorded in the lab notebook and were measured in
Data from Table 1. confirms the theory that as the concentration of glucose increases so will the absorbance of the solution when examined with the glucose oxidase/horseradish peroxidase assay. Glucose within the context of this assay is determined by the amount of ferricyanide, determined by absornace, which is produced in a one to one ratio.1 Furthermore when examining the glucose standards, a linear calibration curve was able to be produced (shown as Figure 1). Noted the R2 value of the y = 1.808x - 0.0125 trend line is 0.9958, which is statistically considered linear. From this calibration curve the absorbance values of unknowns samples can be compared, and the correlated glucose concentration can then be approximated.
In the lab, Inhibiting the Action of Catechol Oxidase we had to investigate what type of enzyme inhibition occurs when an inhibitor is added. Catechol oxidase is an enzyme in plants that creates benzoquinone.Benzoquinone is a substance that is toxic to bacteria. It is brown and is the reason fruit turns brown. Now, there are two types of inhibitors, the competitive inhibitor and non-competitive inhibitor. For an enzyme reaction to occur a substrate has to bind or fit into the active site of the enzyme. In competitive inhibition there is a substrate and an inhibitor present, both compete to bind to the active site. If the competitive inhibitor binds to the active site it stops the reaction. A noncompetitive inhibitor binds to another region
Living organisms undergo chemical reactions with the help of unique proteins known as enzymes. Enzymes significantly assist in these processes by accelerating the rate of reaction in order to maintain life in the organism. Without enzymes, an organism would not be able to survive as long, because its chemical reactions would be too slow to prolong life. The properties and functions of enzymes during chemical reactions can help analyze the activity of the specific enzyme catalase, which can be found in bovine liver and yeast. Our hypothesis regarding enzyme activity is that the aspects of biology and environmental factors contribute to the different enzyme activities between bovine liver and yeast.
Catalase is a common enzyme that is produced in all living organisms. All living organisms are made up of cells and within the cells, enzymes function to increase the rate of chemical reactions. Enzymes function to create the same reactions using a lower amount of energy. The reactions of catalase play an important role to life, for example, it breaks down hydrogen peroxide into oxygen and water. Our group developed an experiment to test the rate of reaction of catalase in whole carrots and pinto beans with various concentrations of hydrogen peroxide. Almost all enzymes are proteins and proteins are made up of amino acids. The areas within an enzyme speed up the chemical reactions which are known as the active sites, and are also where the
The purpose of this experiment was to see if phenylthiourea (PTU) is a non-competitive or competitive inhibitor. Catechol, a phenolic compound found in the potato extract used will play the part of the substrate. Competitive inhibitors are known to bind to the active site of an enzyme and mimic the job of a substrate. This in turn causes the substrate to compete for a position at the active site and increase the concentration of substrate but the inhibitor is still at a constant level. If PTU were a competitive inhibitor the test tube carrying the extract would turn dark brown. Non- competitive inhibitors are known to bind on the enzyme and prevent the substrate from attaching
The purpose of this experiment was to discover the specificity of the enzyme lactase to a spec...
EDTA, the chelating agent that binds with magnesium, had a high absorbency and strong color change to red. The correct cofactor was copper which with the chelating agent of PTU and citric acid which both bind strongly to copper which keeps it from binding with the enzyme. This was determined because in the trails, both PTU and citric acid had low absorbency and were clear or roughly clear in color. The catechol in each tube, which was the control for this experiment, allowed the cofactor that would be used in this reaction to be singled out. The way each chelating agent would affect the different cofactors displayed which was not needed for the reaction and which cofactors were needed for the reaction. An inconsistency that may have affected the data would be if the calibration tube malfunctioned in balancing the spectrophotometer to zero. There also could be errors if the calibration tube wasn’t used before each tube was tested in the spectrophotometer. The relationship of the cofactor and amount of enzyme activity would be that if the cofactor is inhibited or not, the enzyme activity would be higher if the cofactor is not inhibited but lower if it was inhibited by the chelating
The independent variable for this experiment is the enzyme concentration, and the range chosen is from 1% to 5% with the measurements of 1, 2, 4, and 5%. The dependant variable to be measured is the absorbance of the absorbance of the solution within a colorimeter, Equipments: Iodine solution: used to test for present of starch - Amylase solution - 1% starch solution - 1 pipette - 3 syringes - 8 test tubes – Stop clock - Water bath at 37oc - Distilled water- colorimeter Method: = == ==
The reaction will increase with the increasing enzyme concentration when the molecules of hydrogen peroxide are freely available. The more concentrated the catalase the more chance of the
Enzyme peroxidase is essential in any cell metabolic reaction as it breaks down the harmful hydrogen peroxide to harmful products in the body. The report analyzed its effect on changes in temperatures by determining the optimum temperatures and the effects of its reversibility. Through the method of extracting the enzyme by blending it with potato tissue in phosphate buffer, the effects were analyzed on the effect of the dye guaiacol and the activity measured under different temperatures. The optimum temperature was obtained at 22.20C and above this temperature, the enzyme was denatured. Conclusively, increase in temperature increases
In this experiment the enzyme peroxidase and the substrate hydrogen peroxide were not mixed initially, instead they were both placed in separate tubes and were incubated at a specific temperature, to prevent hydrogen peroxide from undergoing any reaction with peroxidase until they both acquire the required temperature.
Abstract: Enzymes are catalysts therefore we can state that they work to start a reaction or speed it up. The chemical transformed due to the enzyme (catalase) is known as the substrate. In this lab the chemical used was hydrogen peroxide because it can be broken down by catalase. The substrate in this lab would be hydrogen peroxide and the enzymes used will be catalase which is found in both potatoes and liver. This substrate will fill the active sites on the enzyme and the reaction will vary based on the concentration of both and the different factors in the experiment. Students placed either liver or potatoes in test tubes with the substrate and observed them at different temperatures as well as with different concentrations of the substrate. Upon reviewing observations, it can be concluded that liver contains the greater amount of catalase as its rates of reaction were greater than that of the potato.
15ml of Buffer Solution at pH 8.4 produced the amount of oxygen required in 0.44cm³ per second. On the other hand, 15ml of Buffer Solution at pH 4.4 produced this amount of oxygen in 1.45cm³ per second. We can clearly see that when the Buffer Solution's pH concentration is increased, this has the same effect on the speed of the reaction, which is the effect of pH on the
Hypothesis: If a test tube filled with 3% hydrogen peroxide and catalase solution, the room temperature will increase the activity. Freezer, refrigerator, and boiling water will have
The temperature of the water shows if the temperature in which catalase reacts in has an effect on the amount of oxygen produced. Every enzyme has an optimum amount of pH, which allows it to have a higher reaction velocity (WBC).The higher the reaction velocity the more reactive the enzyme is. Measuring the different amount of pH solutions and their effect on the amount of oxygen produced can show the optimum pH for catalase and the effect pH has on catalase. The data that these three independent variables will yield will allow us to better understand the effects concentration, temperature and pH have on the enzyme catalase. If catalase reacts at full concentration, 37 degrees celsius and a pH of eight the enzyme catalase will produce more oxygen than if it is at room temperature, a lower concentration and a more acidic base because the higher temperature will allow molecules to move faster and have a higher chance to collide and react, a higher concentration will create a higher enzyme to substrate ratio which allows it to react more and finally a more basic pH will allow it catalase to have a higher reaction